Pub Date : 2014-08-20DOI: 10.2142/BIOPHYS.54.S210_2
Tetsunari Kimura, Shoko Ishii, T. Tosha, Y. Shiro, M. Kubo
{"title":"2P092 Characterization of transient NO-bound form of Nitric Oxide Reductase by Transient Absorption Spectroscopy(02. Heme proteins,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"Tetsunari Kimura, Shoko Ishii, T. Tosha, Y. Shiro, M. Kubo","doi":"10.2142/BIOPHYS.54.S210_2","DOIUrl":"https://doi.org/10.2142/BIOPHYS.54.S210_2","url":null,"abstract":"","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"49 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2014-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"114331293","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2014-08-20DOI: 10.2142/biophys.54.S171_6
Chien-Jung Lo, Meiting Chen
{"title":"1P186 Direct measurement of Vibrio alginolyticus polar flagellum growth rate(12. Cell biology,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"Chien-Jung Lo, Meiting Chen","doi":"10.2142/biophys.54.S171_6","DOIUrl":"https://doi.org/10.2142/biophys.54.S171_6","url":null,"abstract":"","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"43 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2014-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"123684350","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2014-08-20DOI: 10.2142/biophys.54.S330_1
G. Kurisu
{"title":"Modifications to the Protein Data Bank : A new PDB format, Data Deposition, and Validation Report(PDBj: Protein Data Bank Japan,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"G. Kurisu","doi":"10.2142/biophys.54.S330_1","DOIUrl":"https://doi.org/10.2142/biophys.54.S330_1","url":null,"abstract":"","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"51 4 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2014-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"116831781","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2014-08-20DOI: 10.2142/BIOPHYS.54.S240_2
Koya Kato, G. Chikenji
{"title":"2P272 A Ligand Based Virtual Screening method that takes into account of protein-ligand interactions(22A. Bioinformatics:Structural genomics,Poster)","authors":"Koya Kato, G. Chikenji","doi":"10.2142/BIOPHYS.54.S240_2","DOIUrl":"https://doi.org/10.2142/BIOPHYS.54.S240_2","url":null,"abstract":"","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"200 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2014-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"124477007","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2014-08-20DOI: 10.2142/biophys.54.S294_2
Z. Kalay, Y. Yoshinari, Y. Harada
{"title":"3P272 Observing the rotational diffusion of nanodiamonds with arbitrary nitrogen vacancy center configurations(24. Mathematical biology,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"Z. Kalay, Y. Yoshinari, Y. Harada","doi":"10.2142/biophys.54.S294_2","DOIUrl":"https://doi.org/10.2142/biophys.54.S294_2","url":null,"abstract":"","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"45 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2014-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"128184197","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2014-08-20DOI: 10.2142/BIOPHYS.54.S204_2
Tomoko Kunihara, Yuuki Hayashi, M. Arai
{"title":"2P056 Interaction of the intrinsically disordered HIV-1 Tat protein with the KIX domain of the transcriptional coactivator CBP(01C. Protein: Property,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"Tomoko Kunihara, Yuuki Hayashi, M. Arai","doi":"10.2142/BIOPHYS.54.S204_2","DOIUrl":"https://doi.org/10.2142/BIOPHYS.54.S204_2","url":null,"abstract":"","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"183 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2014-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"127025658","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2014-08-20DOI: 10.2142/BIOPHYS.54.S122_3
N. Suematsu
{"title":"1SCP-04 Self-propelled water droplet coupled with chemical oscillatory reaction(1SCP Nonlinear physico-chemical systems moving like living organisms,Symposium,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"N. Suematsu","doi":"10.2142/BIOPHYS.54.S122_3","DOIUrl":"https://doi.org/10.2142/BIOPHYS.54.S122_3","url":null,"abstract":"","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"76 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2014-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"128865809","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2014-08-20DOI: 10.2142/BIOPHYS.54.S124_4
Ryang Kim, Mio Nonaka, Nan Yagishita-Kyo, T. Kawashima, Masatoshi Inoue, Yuichiro Ishii, Toshihiro Endo, Hajime Fujii, S. Takemoto-Kimura, H. Okuno, H. Bito
Ca 2+ /Calmodulin-dependent kinase II (CaMKII) is one of the most important signaling molecules for synaptic plasticity underlying learning and memory. Here, we developed a photo-activatable CaMKII (paCaMKII). Light-induced spine specific CaMKII activation successfully induced the structural plasticity, which suggesting that CaMKII activation is sufficient for the plasticity. In addition, we imaged the activity of Rho GTPases, RhoA and Cdc42, by using 2pFLIM and found that these molecules are activated via CaMKII. Furthermore, since the loss of function assay suggests that RhoA and Cdc42 works for triggering and maintaining the structural plasticity, respectively, these molecules may cooperatively work for establishing the spine structural plasticity. The plasma membrane (PM) of neuronal cells is split into two regions with distinct functions, the somatodendritic domain (neuronal signal input) and axon (output). Many PM molecules reside in either one of the two domains, which is enabled by the presence of a diffusion barrier in the PM in the initial segment (IS) region, the interface between the two domains. The diffusion barrier is formed by the cooperative assembly and binding of transmembrane proteins and scaffolding actin-binding molecules. Recently, we found that the diffusion barrier is a molecule-selective filter, allowing GPI-anchored proteins to pass through, but not transmembrane proteins and phospholipids. The mechanism for the selective passage is becoming clear, which will be discussed in this talk. Long-term memory formation requires a complex coordination of signaling to enable specific storage of otherwise transient information acquired as memory events happen. How does such conversion from labile into a more stable information occur? We here our recent on multiple levels of signal cooperation, at the synaptic, dendritic and nuclear compartments of a neuron, which together contribute to achieving this formidable signal processing. Recent human genome sequencing studies indicate that maladaptation of such signaling cascades may underlie several forms of
ca2 + /Calmodulin-dependent kinase II (CaMKII)是影响学习和记忆突触可塑性的重要信号分子之一。在这里，我们开发了一种光活化CaMKII (paCaMKII)。光诱导的脊柱特异性CaMKII激活成功诱导了结构可塑性，这表明CaMKII激活是可塑性的充分条件。此外，我们利用2pFLIM对Rho GTPases、RhoA和Cdc42的活性进行了成像，发现这些分子通过CaMKII被激活。此外，由于功能丧失实验表明RhoA和Cdc42分别用于触发和维持结构可塑性，因此这些分子可能共同作用于脊柱结构可塑性的建立。神经元细胞的质膜(PM)分为两个功能不同的区域，即体突区域(神经元信号输入)和轴突区域(神经元信号输出)。许多PM分子驻留在两个结构域中的任何一个，这是由于PM在初始段(is)区域(两个结构域之间的界面)中存在扩散屏障而实现的。扩散屏障是由跨膜蛋白和支架肌动蛋白结合分子的协同组装和结合形成的。最近，我们发现扩散屏障是一个分子选择性过滤器，允许gpi锚定蛋白通过，但不允许跨膜蛋白和磷脂通过。选择性通道的机制越来越清晰，这将在本次演讲中讨论。长期记忆的形成需要复杂的信号协调，以使记忆事件发生时获得的短暂信息能够特定存储。这种从不稳定信息到更稳定信息的转换是如何发生的?在此，我们在神经元的突触、树突和核区室的信号合作的多个层面上进行了最新的研究，它们共同有助于实现这种强大的信号处理。最近的人类基因组测序研究表明，这种信号级联的不适应可能是几种形式的疾病的基础
{"title":"1SEP-04 Activity-dependent gene expression in learning and memory(1SEP Cooperativity in shaping the nerve cell function,Symposium,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"Ryang Kim, Mio Nonaka, Nan Yagishita-Kyo, T. Kawashima, Masatoshi Inoue, Yuichiro Ishii, Toshihiro Endo, Hajime Fujii, S. Takemoto-Kimura, H. Okuno, H. Bito","doi":"10.2142/BIOPHYS.54.S124_4","DOIUrl":"https://doi.org/10.2142/BIOPHYS.54.S124_4","url":null,"abstract":"Ca 2+ /Calmodulin-dependent kinase II (CaMKII) is one of the most important signaling molecules for synaptic plasticity underlying learning and memory. Here, we developed a photo-activatable CaMKII (paCaMKII). Light-induced spine specific CaMKII activation successfully induced the structural plasticity, which suggesting that CaMKII activation is sufficient for the plasticity. In addition, we imaged the activity of Rho GTPases, RhoA and Cdc42, by using 2pFLIM and found that these molecules are activated via CaMKII. Furthermore, since the loss of function assay suggests that RhoA and Cdc42 works for triggering and maintaining the structural plasticity, respectively, these molecules may cooperatively work for establishing the spine structural plasticity. The plasma membrane (PM) of neuronal cells is split into two regions with distinct functions, the somatodendritic domain (neuronal signal input) and axon (output). Many PM molecules reside in either one of the two domains, which is enabled by the presence of a diffusion barrier in the PM in the initial segment (IS) region, the interface between the two domains. The diffusion barrier is formed by the cooperative assembly and binding of transmembrane proteins and scaffolding actin-binding molecules. Recently, we found that the diffusion barrier is a molecule-selective filter, allowing GPI-anchored proteins to pass through, but not transmembrane proteins and phospholipids. The mechanism for the selective passage is becoming clear, which will be discussed in this talk. Long-term memory formation requires a complex coordination of signaling to enable specific storage of otherwise transient information acquired as memory events happen. How does such conversion from labile into a more stable information occur? We here our recent on multiple levels of signal cooperation, at the synaptic, dendritic and nuclear compartments of a neuron, which together contribute to achieving this formidable signal processing. Recent human genome sequencing studies indicate that maladaptation of such signaling cascades may underlie several forms of","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"47 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2014-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"126722431","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2014-08-20DOI: 10.2142/BIOPHYS.54.S185_4
T. Kunisawa
{"title":"1P268 Evolutionary Relationships of Clostridia Species(22D. Bioinformatics:Molecular evolution,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"T. Kunisawa","doi":"10.2142/BIOPHYS.54.S185_4","DOIUrl":"https://doi.org/10.2142/BIOPHYS.54.S185_4","url":null,"abstract":"","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"33 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2014-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"126837876","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
京公网安备 11010802042870号
京ICP备2023020795号-1
扫码关注我们
求助内容：
应助结果提醒方式：